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Q87D63 (GCH1_XYLFT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
Gene names
Name:folE
Ordered Locus Names:PD_0823
OrganismXylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]
Taxonomic identifier183190 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_00223

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_00223

Subunit structure

Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence caution

The sequence AAO28691.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203GTP cyclohydrolase 1 HAMAP-Rule MF_00223
PRO_0000119469

Sites

Metal binding871Zinc By similarity
Metal binding901Zinc By similarity
Metal binding1581Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87D63 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 542FBCC67FC4B1BB

FASTA20322,983
        10         20         30         40         50         60 
MDHSKQQNAS ITQAQAEEAV RTLLRWAGED PTREGLLDTP RRVVEAYGDW FSGYREDPHD 

        70         80         90        100        110        120 
YLQRTFEEIS CYDEMIVLRN ITYESHCEHH MAPIIGKVHV GYLPNGKVVG ISKLARVVES 

       130        140        150        160        170        180 
YARRFQIQEK MTAQIAACIQ DTLTPRGVGV VIEGAHACMT TRGIHKRGVS MVTSKMLGTF 

       190        200 
REDARTRAEF LQFIEVGTNV IDL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009442 Genomic DNA. Translation: AAO28691.1. Different initiation.
RefSeqNP_779042.1. NC_004556.1.

3D structure databases

ProteinModelPortalQ87D63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING183190.PD0823.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO28691; AAO28691; PD_0823.
GeneID1143545.
KEGGxft:PD0823.
PATRIC24149519. VBIXylFas71109_1073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0302.
KOK01495.
OMAVIVVTEC.
OrthoDBEOG6XHC8G.
ProtClustDBPRK09347.

Enzyme and pathway databases

BioCycXFAS183190:GIX4-823-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_00223. FolE.
InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsTIGR00063. folE. 1 hit.
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCH1_XYLFT
AccessionPrimary (citable) accession number: Q87D63
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways